NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|440538807|emb|CCP64321|]
View 

lipoate-protein ligase A [Chlamydia trachomatis L1/115]

Protein Classification

lipoate--protein ligase family protein( domain architecture ID 11612796)

lipoate--protein ligase (LPL) family protein is responsible for attaching lipoic acid to a specific lysine at the active site of lipoate-dependent enzymes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
5-203 5.09e-61

lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.


:

Pssm-ID: 319742  Cd Length: 209  Bit Score: 190.16  E-value: 5.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807   5 CVFVHCEGLPIFKQLQLEEALLRTSSQNFCLVN--THLPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDA 82
Cdd:cd16443    1 MRLIDSSGDPPAENLALDEALLRSVAAPPTLRLylWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRPSGGGAVFHDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  83 DSLMVSWIINSPTPS--PSSKDLLQWTQDIYAPIFPTGF--KITENDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPK 158
Cdd:cd16443   81 GNLNYSLILPKEHPSidESYRALSQPVIKALRKLGVEAEfgGVGRNDLVVGGKKISGSAQRRTKGRILHHGTLLVDVDLE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 440538807 159 KLARYLPTPEIQPSYRQNRSHDEFLTTIYEL---FDSREDFLSQLKQS 203
Cdd:cd16443  161 KLARVLNVPYEKLKSKGPKSVRSRVTNLSELlgrDITVEEVKNALLEA 208
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
5-203 5.09e-61

lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.


Pssm-ID: 319742  Cd Length: 209  Bit Score: 190.16  E-value: 5.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807   5 CVFVHCEGLPIFKQLQLEEALLRTSSQNFCLVN--THLPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDA 82
Cdd:cd16443    1 MRLIDSSGDPPAENLALDEALLRSVAAPPTLRLylWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRPSGGGAVFHDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  83 DSLMVSWIINSPTPS--PSSKDLLQWTQDIYAPIFPTGF--KITENDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPK 158
Cdd:cd16443   81 GNLNYSLILPKEHPSidESYRALSQPVIKALRKLGVEAEfgGVGRNDLVVGGKKISGSAQRRTKGRILHHGTLLVDVDLE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 440538807 159 KLARYLPTPEIQPSYRQNRSHDEFLTTIYEL---FDSREDFLSQLKQS 203
Cdd:cd16443  161 KLARVLNVPYEKLKSKGPKSVRSRVTNLSELlgrDITVEEVKNALLEA 208
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
21-203 3.74e-33

Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 439865  Cd Length: 246  Bit Score: 119.95  E-value: 3.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  21 LEEALLRTSSQN------FCLVNthlPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINSP 94
Cdd:COG0095   16 LDEALLEEVAEGedpptlRLWRN---PPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDPGNLNYSLILPED 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  95 TPSPSSKD----LLQWTQDIYAPIfptGFKIT---ENDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYLPTP 167
Cdd:COG0095   93 DVPLSIEEsyrkLLEPILEALRKL---GVDAEfsgRNDIVVDGRKISGNAQRRRKGAVLHHGTLLVDGDLEKLAKVLRVP 169
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440538807 168 EIQPSYRQNRSHDEFLTTIYELFD---SREDFLSQLKQS 203
Cdd:COG0095  170 YEKLRDKGIKSVRSRVTNLSELLGtdiTREEVKEALLEA 208
PRK14061 PRK14061
unknown domain/lipoate-protein ligase A fusion protein; Provisional
42-164 3.08e-07

unknown domain/lipoate-protein ligase A fusion protein; Provisional


Pssm-ID: 172552 [Multi-domain]  Cd Length: 562  Bit Score: 50.49  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  42 EAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINSPT--PSPSSKDLLQWTQDIYAPIFPTGf 119
Cdd:PRK14061 266 DTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEydKTISTSIVLNALNALGVSAEASG- 344
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 440538807 120 kitENDYTFL----DKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYL 164
Cdd:PRK14061 345 ---RNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYL 390
 
Name Accession Description Interval E-value
LplA cd16443
lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide ...
5-203 5.09e-61

lipoate-protein ligase; Lipoate-protein ligase A (LplA) catalyzes the formation of an amide linkage between free lipoic acid and a specific lysine residue of the lipoyl domain in lipoate dependent enzymes, similar to the biotinylation reaction mediated by biotinyl protein ligase (BPL). The two step reaction includes activation of exogenously supplied lipoic acid at the expense of ATP to lipoyl-AMP and then transfer to the epsilon-amino group of a specific lysine residue of the lipoyl domain of the target protein.


Pssm-ID: 319742  Cd Length: 209  Bit Score: 190.16  E-value: 5.09e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807   5 CVFVHCEGLPIFKQLQLEEALLRTSSQNFCLVN--THLPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDA 82
Cdd:cd16443    1 MRLIDSSGDPPAENLALDEALLRSVAAPPTLRLylWQNPPTVVIGRFQNPLEEVNLEYAEEDGIPVVRRPSGGGAVFHDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  83 DSLMVSWIINSPTPS--PSSKDLLQWTQDIYAPIFPTGF--KITENDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPK 158
Cdd:cd16443   81 GNLNYSLILPKEHPSidESYRALSQPVIKALRKLGVEAEfgGVGRNDLVVGGKKISGSAQRRTKGRILHHGTLLVDVDLE 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 440538807 159 KLARYLPTPEIQPSYRQNRSHDEFLTTIYEL---FDSREDFLSQLKQS 203
Cdd:cd16443  161 KLARVLNVPYEKLKSKGPKSVRSRVTNLSELlgrDITVEEVKNALLEA 208
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
21-203 3.74e-33

Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 439865  Cd Length: 246  Bit Score: 119.95  E-value: 3.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  21 LEEALLRTSSQN------FCLVNthlPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINSP 94
Cdd:COG0095   16 LDEALLEEVAEGedpptlRLWRN---PPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDPGNLNYSLILPED 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  95 TPSPSSKD----LLQWTQDIYAPIfptGFKIT---ENDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYLPTP 167
Cdd:COG0095   93 DVPLSIEEsyrkLLEPILEALRKL---GVDAEfsgRNDIVVDGRKISGNAQRRRKGAVLHHGTLLVDGDLEKLAKVLRVP 169
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440538807 168 EIQPSYRQNRSHDEFLTTIYELFD---SREDFLSQLKQS 203
Cdd:COG0095  170 YEKLRDKGIKSVRSRVTNLSELLGtdiTREEVKEALLEA 208
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
17-190 7.05e-08

biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.


Pssm-ID: 319740  Cd Length: 198  Bit Score: 51.00  E-value: 7.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  17 KQLQLEEALLR---TSSQNFCLVNTHlPEAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINS 93
Cdd:cd16435   12 SAWAAQEKSLRenvSNQSSTLLLWEH-PTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPGQLVFSPVIGP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  94 PTPSPSSKDLLQWT-------QDIYAPIFPTGFKiteNDYTFLDKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYLPt 166
Cdd:cd16435   91 NVEFMISKFNLIIEegirdaiADFGQSAEVKWGR---NDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQDLENFTEIIP- 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 440538807 167 PEIQPSYRQNRS--------HDEFLTTIYELF 190
Cdd:cd16435  167 CGYKPERVTSLSlelgrkvtVEQVLERVLAAF 198
PRK14061 PRK14061
unknown domain/lipoate-protein ligase A fusion protein; Provisional
42-164 3.08e-07

unknown domain/lipoate-protein ligase A fusion protein; Provisional


Pssm-ID: 172552 [Multi-domain]  Cd Length: 562  Bit Score: 50.49  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  42 EAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINSPT--PSPSSKDLLQWTQDIYAPIFPTGf 119
Cdd:PRK14061 266 DTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEydKTISTSIVLNALNALGVSAEASG- 344
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 440538807 120 kitENDYTFL----DKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYL 164
Cdd:PRK14061 345 ---RNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYL 390
lplA PRK03822
lipoate-protein ligase A; Provisional
42-164 3.60e-06

lipoate-protein ligase A; Provisional


Pssm-ID: 179655  Cd Length: 338  Bit Score: 46.99  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440538807  42 EAVVLGISRKPERDLHVEHLKEDGIPIIRRYSGGGTVFLDADSLMVSWIINSP--TPSPSSKDLLQWTQDIYAPIFPTGf 119
Cdd:PRK03822  42 DTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPeyDKTISTSIVLNALNSLGVSAEASG- 120
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 440538807 120 kitENDYTFL----DKKIGGNAQYIQKYRWVHHTTFLWNMNPKKLARYL 164
Cdd:PRK03822 121 ---RNDLVVKtaegDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYL 166
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH